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A histone octamer-like structure within TFIID

Nature volume 380, pages 356–359 (1996)Cite this article

Abstract

THE general transcription factor TFIID nucleates initiation complex formation through direct core promoter binding1,2, commits promoters within chromatin to transcription3, and mediates the action of transcriptional activators, a phenomenon that may correlate with enhanced TFIID recruitment4–7 or conformational changes in TFIID-promoter complexes8,9. Molecular studies of the multiprotein TFIID complex have identified a primary TATA binding subunit (TBP)2, TBP-associated factors (TAFs) that interact with and mediate the function of activators2,7,10,11 and intersubunit interactions2 but have yielded relatively little insight into the structural organization of the complex or the actual mechanism of transcriptional activation. Here we present biochemical evidence for the structural relevance of histone homo-logies in the human TFIID subunits hTAFSO, hTAF31 and hTAF20/15. Together with analyses of native TFIID complexes and accompanying crystallographic studies12, the results suggest that there is a histone octamer-like TAF complex within TFIID.

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Author notes

  1. Alexander Hoffmann

    Present address: Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts, 02139, USA

  2. Cheng-Ming Chiang

    Present address: Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois, 61801, USA

Authors and Affiliations

  1. Laboratory of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, New York, 10021, USA

    Alexander Hoffmann, Cheng-Ming Chiang, Thomas Oelgeschläger & Robert G. Roeder

  2. Laboratories of Molecular Biophysics, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, New York, 10021, USA

    Xiaoling Xie & Stephen K. Burley

  3. National Institute of Child Health and Human Development and National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, 20892, USA

    Yoshihiro Nakatani

Authors
  1. Alexander Hoffmann
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Hoffmann, A., Chiang, CM., Oelgeschläger, T. et al. A histone octamer-like structure within TFIID. Nature 380, 356–359 (1996). https://doi.org/10.1038/380356a0

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